|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
2-628 |
0e+00 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 976.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 2 EYELLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHK 81
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 82 LITGRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMN 161
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGED-RKVVAVIGDGALTGGMAFEALN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 162 NAVGLKKDILVILNDNQMGICPRVGGLATYLDNARVAPFYNGLKRDIAWALNKVPMVGNSVEHALSNMKDAVKTLLHGGR 241
Cdd:COG1154 160 NAGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 242 LFEEMGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDRtDDGDAIPrPKGSVP 321
Cdd:COG1154 240 LFEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDP-ETGEPKK-SKSSAP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 322 AYTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRS 401
Cdd:COG1154 318 SYTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 402 FDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHDGPISIRYPKAN 481
Cdd:COG1154 398 YDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 482 AVTVERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVV 561
Cdd:COG1154 478 GPGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVV 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503394266 562 TVEENTLCGGFGSTVLEAANDAGLPTnNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQLAK 628
Cdd:COG1154 558 TVEEGVLAGGFGSAVLEFLADAGLDV-PVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-626 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 851.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 1 MEYELLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPH 80
Cdd:PRK05444 2 PKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 81 KLITGRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDGRKSVAVIGDGALPSGVVFEAM 160
Cdd:PRK05444 82 KILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 161 NNAVGLKKDILVILNDNQMGICPRVGGLATYLDNARvapfynglkrdiawalnkvpmvgnsvehalSNMkdavktllhgg 240
Cdd:PRK05444 162 NNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLR------------------------------SST----------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 241 rLFEEMGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDRTDdGDAIPRPKGSV 320
Cdd:PRK05444 201 -LFEELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPET-GEQPKSSKPGK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 321 PAYTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQR 400
Cdd:PRK05444 279 PSYTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 401 SFDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEH-DGPISIRYPK 479
Cdd:PRK05444 359 AYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYdDGPIAIRYPR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 480 ANAVTVEREnEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQkdglDVGVINARFLRPLDTDVILKAVRECGF 559
Cdd:PRK05444 439 GNGVGVELP-ELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDL 513
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503394266 560 VVTVEENTLCGGFGSTVLEAANDAGLPTnNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQL 626
Cdd:PRK05444 514 VVTVEEGAIMGGFGSAVLEFLADHGLDV-PVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILEL 579
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
6-626 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129308 [Multi-domain] Cd Length: 617 Bit Score: 674.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 6 LPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLITG 85
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 86 RFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMNNAVG 165
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGAD-RKTVCVIGDGAITAGMAFEALNHAGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 166 LKKDILVILNDNQMGICPRVGGLATYLDNARVAPFYNGLKRDIAWALNKVPMVGNSVehaLSNMKDAVKTLLHGGRLFEE 245
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYL---AKRTEESMKGLVVPGTFFEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 246 MGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDrTDDGDaIPRPKGSVPAYTN 325
Cdd:TIGR00204 237 LGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFD-LSTGC-LPKSKSALPSYSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 326 IASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRSFDHI 405
Cdd:TIGR00204 315 IFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 406 FQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHD-GPISIRYPKANAVT 484
Cdd:TIGR00204 395 VHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDdGPIAVRYPRGNAVG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 485 VERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVVTVE 564
Cdd:TIGR00204 475 VELTPEPEKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVE 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503394266 565 ENTLCGGFGSTVLEAANDAGLPTnNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQL 626
Cdd:TIGR00204 555 ENAIMGGAGSAVLEFLMDQNKLV-PVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAW 615
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
6-282 |
8.74e-143 |
|
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).
Pssm-ID: 463832 [Multi-domain] Cd Length: 274 Bit Score: 416.04 E-value: 8.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 6 LPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLITG 85
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 86 RFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMNNAVG 165
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGED-RKVVAVIGDGALTGGMAFEALNNAGH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 166 LKKDILVILNDNQMGICPRVGGLATYLDNARVAPFYNGLKRDIAWALNkvPMVGNSVEHALSNMKDAVKTLLHGGRLFEE 245
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEE 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 503394266 246 MGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFT 282
Cdd:pfam13292 238 LGFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
43-288 |
7.13e-98 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 297.54 E-value: 7.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 43 AHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLITGRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASV 122
Cdd:cd02007 2 GHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 123 STVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMNNAVGLKKDILVILNDNQMGICPRVGglatyldnarvapfyn 202
Cdd:cd02007 82 SAALGMAVARDLKGKK-RKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 203 glkrdiawalnkvpmvgnsvehalsnmkdavktllHGGRLFEEMGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFT 282
Cdd:cd02007 145 -----------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVT 189
|
....*.
gi 503394266 283 EKGKGF 288
Cdd:cd02007 190 KKGKGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
366-478 |
7.88e-41 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 144.94 E-value: 7.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 366 FDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRSFDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTF 445
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110
....*....|....*....|....*....|...
gi 503394266 446 PNITVMAPGDTADLQAMIPFSLEHDGPISIRYP 478
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
2-628 |
0e+00 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 976.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 2 EYELLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHK 81
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 82 LITGRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMN 161
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGED-RKVVAVIGDGALTGGMAFEALN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 162 NAVGLKKDILVILNDNQMGICPRVGGLATYLDNARVAPFYNGLKRDIAWALNKVPMVGNSVEHALSNMKDAVKTLLHGGR 241
Cdd:COG1154 160 NAGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 242 LFEEMGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDRtDDGDAIPrPKGSVP 321
Cdd:COG1154 240 LFEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDP-ETGEPKK-SKSSAP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 322 AYTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRS 401
Cdd:COG1154 318 SYTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 402 FDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHDGPISIRYPKAN 481
Cdd:COG1154 398 YDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 482 AVTVERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVV 561
Cdd:COG1154 478 GPGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVV 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503394266 562 TVEENTLCGGFGSTVLEAANDAGLPTnNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQLAK 628
Cdd:COG1154 558 TVEEGVLAGGFGSAVLEFLADAGLDV-PVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-626 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 851.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 1 MEYELLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPH 80
Cdd:PRK05444 2 PKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 81 KLITGRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDGRKSVAVIGDGALPSGVVFEAM 160
Cdd:PRK05444 82 KILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 161 NNAVGLKKDILVILNDNQMGICPRVGGLATYLDNARvapfynglkrdiawalnkvpmvgnsvehalSNMkdavktllhgg 240
Cdd:PRK05444 162 NNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLR------------------------------SST----------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 241 rLFEEMGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDRTDdGDAIPRPKGSV 320
Cdd:PRK05444 201 -LFEELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPET-GEQPKSSKPGK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 321 PAYTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQR 400
Cdd:PRK05444 279 PSYTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 401 SFDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEH-DGPISIRYPK 479
Cdd:PRK05444 359 AYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYdDGPIAIRYPR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 480 ANAVTVEREnEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQkdglDVGVINARFLRPLDTDVILKAVRECGF 559
Cdd:PRK05444 439 GNGVGVELP-ELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDL 513
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503394266 560 VVTVEENTLCGGFGSTVLEAANDAGLPTnNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQL 626
Cdd:PRK05444 514 VVTVEEGAIMGGFGSAVLEFLADHGLDV-PVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILEL 579
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
6-626 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129308 [Multi-domain] Cd Length: 617 Bit Score: 674.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 6 LPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLITG 85
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 86 RFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMNNAVG 165
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGAD-RKTVCVIGDGAITAGMAFEALNHAGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 166 LKKDILVILNDNQMGICPRVGGLATYLDNARVAPFYNGLKRDIAWALNKVPMVGNSVehaLSNMKDAVKTLLHGGRLFEE 245
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYL---AKRTEESMKGLVVPGTFFEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 246 MGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDrTDDGDaIPRPKGSVPAYTN 325
Cdd:TIGR00204 237 LGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFD-LSTGC-LPKSKSALPSYSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 326 IASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRSFDHI 405
Cdd:TIGR00204 315 IFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 406 FQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHD-GPISIRYPKANAVT 484
Cdd:TIGR00204 395 VHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDdGPIAVRYPRGNAVG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 485 VERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVVTVE 564
Cdd:TIGR00204 475 VELTPEPEKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVE 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503394266 565 ENTLCGGFGSTVLEAANDAGLPTnNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQL 626
Cdd:TIGR00204 555 ENAIMGGAGSAVLEFLMDQNKLV-PVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAW 615
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-637 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 614.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 5 LLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLIT 84
Cdd:PRK12571 8 LLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPHKILT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 85 GRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDGRkSVAVIGDGALPSGVVFEAMNNAV 164
Cdd:PRK12571 88 GRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGD-VVAVIGDGSLTAGMAYEALNNAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 165 GLKKDILVILNDNQMGICPRVGGLATYLDNARVAPFYNGLKRDIAWALNKVPmvgNSVEHALSNMKDAVKTLLHGGRLFE 244
Cdd:PRK12571 167 AADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLP---GPLRDGARRARELVTGMIGGGTLFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 245 EMGFRYIGPVDGHDLDALRKYLEMVKDIK-GPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDrTDDGDAiPRPKGSVPAY 323
Cdd:PRK12571 244 ELGFTYVGPIDGHDMEALLSVLRAARARAdGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFD-VVTGLQ-KKSAPSAPSY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 324 TNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRSFD 403
Cdd:PRK12571 322 TSVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 404 HIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHD-GPISIRYPKANA 482
Cdd:PRK12571 402 QLLHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDdGPIAVRFPRGEG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 483 VTVERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVREcGFVVT 562
Cdd:PRK12571 482 VGVEIPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRH-HIVVI 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503394266 563 VEENTLCGGFGSTVLEAANDAGL--PTNNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQLAKANSDLNEAA 637
Cdd:PRK12571 561 VEEQGAMGGFGAHVLHHLADTGLldGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARLSGVPERE 637
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
5-616 |
6.12e-157 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 467.07 E-value: 6.12e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 5 LLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLIT 84
Cdd:PLN02582 33 LLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKILT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 85 GRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLlfeDGRKS--VAVIGDGALPSGVVFEAMNN 162
Cdd:PLN02582 113 GRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDL---KGKKNnvVAVIGDGAMTAGQAYEAMNN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 163 AVGLKKDILVILNDNQM---------GICPRVGGLATYLDNARVAPFYNGLkRDIAWALNKvpMVGNSVEHALSNMKDAV 233
Cdd:PLN02582 190 AGYLDSDMIVILNDNKQvslptatldGPAPPVGALSSALSRLQSSRPLREL-REVAKGVTK--QIGGPMHELAAKVDEYA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 234 KTLLHG--GRLFEEMGFRYIGPVDGHDLDALRKYLEMVKDIK--GPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDRTDD 309
Cdd:PLN02582 267 RGMISGsgSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVVKFDPATG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 310 GDAipRPKGSVPAYTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKP 389
Cdd:PLN02582 347 KQF--KVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 390 IVDIYSTFLQRSFDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLE- 468
Cdd:PLN02582 425 FCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAi 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 469 HDGPISIRYPKANAVTVE--RENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLD 546
Cdd:PLN02582 505 DDRPSCFRYPRGNGIGVQlpPNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLD 584
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503394266 547 TDVILKAVRECGFVVTVEENTLcGGFGSTVLEAANDAGLPTNNIK--RLGIPDRFIEHGNRSELLGELGLDA 616
Cdd:PLN02582 585 RALIRSLAKSHEVLITVEEGSI-GGFGSHVAQFMALDGLLDGKLKwrPLVLPDRYIDHGAPADQLAEAGLTP 655
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-628 |
2.89e-147 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 439.06 E-value: 2.89e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 5 LLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLIT 84
Cdd:PRK12315 2 YLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKMLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 85 GRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDGrKSVAVIGDGALPSGVVFEAMNNAV 164
Cdd:PRK12315 82 GRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKG-NIIAVIGDGSLSGGLALEGLNNAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 165 GLKKDILVILNDNQMGICPRVGGLatyldnarvapfYNGLK--RDiawalnkvpmvgnsvehalSNMKDAvktllhgGRL 242
Cdd:PRK12315 161 ELKSNLIIIVNDNQMSIAENHGGL------------YKNLKelRD-------------------TNGQSE-------NNL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 243 FEEMGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDRTDDGDAIPRPKgsvPA 322
Cdd:PRK12315 203 FKAMGLDYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETGQSKVPASG---ES 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 323 YTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRSF 402
Cdd:PRK12315 280 YSSVTLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 403 DHIFQEVALQNLPVVFCMDRAGLCGPDgPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSL-EHDGPISIRYPkAN 481
Cdd:PRK12315 360 DQLSHDLAINNNPAVMIVFGGSISGND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALtQHEHPVAIRVP-EH 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 482 AVtVERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKD-GLDVGVINARFLRPLDTDVILKAVRECGFV 560
Cdd:PRK12315 438 GV-ESGPTVDTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELLEKLKEDHELV 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503394266 561 VTVEENTLCGGFGSTVleaANDAGLPTNNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQLAK 628
Cdd:PRK12315 517 VTLEDGILDGGFGEKI---ARYYGNSDMKVLNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDILSVLK 581
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
6-282 |
8.74e-143 |
|
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).
Pssm-ID: 463832 [Multi-domain] Cd Length: 274 Bit Score: 416.04 E-value: 8.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 6 LPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLITG 85
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 86 RFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMNNAVG 165
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGED-RKVVAVIGDGALTGGMAFEALNNAGH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 166 LKKDILVILNDNQMGICPRVGGLATYLDNARVAPFYNGLKRDIAWALNkvPMVGNSVEHALSNMKDAVKTLLHGGRLFEE 245
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEE 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 503394266 246 MGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFT 282
Cdd:pfam13292 238 LGFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
5-606 |
4.63e-131 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 399.47 E-value: 4.63e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 5 LLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLIT 84
Cdd:PLN02234 66 LLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 85 GRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDGrKSVAVIGDGALPSGVVFEAMNNAV 164
Cdd:PLN02234 146 GRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNN-SVVSVIGDGAMTAGQAYEAMNNAG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 165 GLKKDILVILNDNQMGICPRVGglatyLDNArvapfynglkrdiawalnkVPMVGnSVEHALSNMKDAVKTLLH-GGRLF 243
Cdd:PLN02234 225 YLHSNMIVILNDNKQVSLPTAN-----LDGP-------------------TQPVG-ALSCALSRLQSNCGMIREtSSTLF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 244 EEMGFRYIGPVDGHDLDALRKYLEMVKDIK--GPTLLHVFTEKGKGFKPASEDPVTFHSPSPFDrTDDGDAIpRPKGSVP 321
Cdd:PLN02234 280 EELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFD-PETGKQF-KNISKTQ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 322 AYTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRS 401
Cdd:PLN02234 358 SYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 402 FDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLE-HDGPISIRYPKA 480
Cdd:PLN02234 438 YDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAiDDRPSCFRYHRG 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 481 NAVTVERE--NEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECG 558
Cdd:PLN02234 518 NGIGVSLPpgNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE 597
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 503394266 559 FVVTVEENTLcGGFGSTVLEAANDAGLPTNNIKrlgIPDRFIEHGNRS 606
Cdd:PLN02234 598 VLITVEEGSI-GGFGSHVVQFLALDGLLDGKLK---VYRTWITNGSTS 641
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
43-288 |
7.13e-98 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 297.54 E-value: 7.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 43 AHFASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPHKLITGRFSRFETIRDRGGLMGFPNPNESPYDLFMTGHAGASV 122
Cdd:cd02007 2 GHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 123 STVLGLQAADDLLFEDgRKSVAVIGDGALPSGVVFEAMNNAVGLKKDILVILNDNQMGICPRVGglatyldnarvapfyn 202
Cdd:cd02007 82 SAALGMAVARDLKGKK-RKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 203 glkrdiawalnkvpmvgnsvehalsnmkdavktllHGGRLFEEMGFRYIGPVDGHDLDALRKYLEMVKDIKGPTLLHVFT 282
Cdd:cd02007 145 -----------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVT 189
|
....*.
gi 503394266 283 EKGKGF 288
Cdd:cd02007 190 KKGKGY 195
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
2-614 |
1.32e-94 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 306.26 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 2 EYELLPMISSPKDLKTLSEPQLERLAAEIREALCQIVERKPAH-FASNLGVVELCLALHLVFDFEKDRLIWDTGHQIYPH 80
Cdd:PLN02225 75 ETPILDSIETPLQLKNLSVKELKLLADEIRTELHSVLWKKTQKsMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 81 KLITGRFSRFETiRDRGGLMGFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDGRkSVAVIGDGALPSGVVFEAM 160
Cdd:PLN02225 155 KVLTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDR-VVAVIDNATITAGQAYEAM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 161 NNAVGLKKDILVILNDNQMGICPR--------VGGLATYLDNARVAPFYNGLkRDIAWALNKvpMVGNSVEHALSNMKDA 232
Cdd:PLN02225 233 SNAGYLDSNMIVILNDSRHSLHPNmeegskasISALSSIMSKIQSSKIFRKF-RELAKAMTK--RIGKGMYEWAAKVDEY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 233 VKTLL--HGGRLFEEMGFRYIGPVDGHDLDALRKYLEMVK--DIKGPTLLHVFTEKGKgfkpaseDPVTFHSPSPFDRTd 308
Cdd:PLN02225 310 ARGMVgpTGSTLFEELGLYYIGPVDGHNIEDLVCVLREVSslDSMGPVLVHVITEENR-------DAETGKNIMVKDRR- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 309 dgdaiprpkgsvpAYTNIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMK 388
Cdd:PLN02225 382 -------------TYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 389 PIVDIYSTFLQRSFDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLE 468
Cdd:PLN02225 449 PFCIIPSAFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAY 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 469 -HDGPISIRYPKANavTVERENEVA---PIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRP 544
Cdd:PLN02225 529 vTDRPVCFRFPRGS--IVNMNYLVPtglPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKP 606
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503394266 545 LDTDVILKAVRECGFVVTVEENTLcGGFGSTVLEAANDAGLPTNNIK--RLGIPDRFIEHGNRSELLGELGL 614
Cdd:PLN02225 607 LDIKLVRDLCQNHKFLITVEEGCV-GGFGSHVAQFIALDGQLDGNIKwrPIVLPDGYIEEASPREQLALAGL 677
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
329-626 |
3.60e-86 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 271.57 E-value: 3.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 329 KTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFL-QRSFDHIFQ 407
Cdd:COG3958 12 EALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYEQIRN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 408 EVALQNLPVVFCMDRAGLC-GPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHDGPISIRYPKANAVTVE 486
Cdd:COG3958 92 DIAYPNLNVKIVGSHAGLSyGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRLGRGAVPVVY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 487 RENEvaPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVVTVEEN 566
Cdd:COG3958 172 DEDY--EFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEH 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 567 TLCGGFGSTVLEAANDAgLPTnNIKRLGIPDRFIEHGNRSELLGELGLDAVGFIREIRQL 626
Cdd:COG3958 250 SIIGGLGSAVAEVLAEN-YPV-PLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKEL 307
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
325-479 |
5.73e-64 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 208.06 E-value: 5.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 325 NIASKTIYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRSFDH 404
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503394266 405 IFQEVALQNLPVVFCMDRAGLC-GPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHDGPISIRYPK 479
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGISvGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
366-478 |
7.88e-41 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 144.94 E-value: 7.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 366 FDTGICEAHAVAFAAGMAKSGMKPIVDIYSTFLQRSFDHIFQEVALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTF 445
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110
....*....|....*....|....*....|...
gi 503394266 446 PNITVMAPGDTADLQAMIPFSLEHDGPISIRYP 478
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
333-600 |
2.25e-36 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 139.00 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 333 DAMERDSKVVVMtaamcaGNDLGRI----------RDDF-PQRFFDTGICEAHAVAFAAGMAKSGMKPIVDI-YSTFLQR 400
Cdd:COG0022 16 EEMERDPRVFVM------GEDVGKYggvfgvtkglQEKFgPDRVFDTPISEAGIVGAAIGAALAGLRPVVEIqFADFIYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 401 SFDHIFQEVA--------LQNLPVVF-CMDRAGLCGpdGPTH----HGVFdntymRTFPNITVMAPGDTAD----LQAMI 463
Cdd:COG0022 90 AFDQIVNQAAklrymsggQFKVPMVIrTPYGGGIGA--GAQHsqslEAWF-----AHIPGLKVVAPSTPYDakglLKAAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 464 ----P--FsLEHDGpisiRYPKANAVTVEREnevaPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVI 537
Cdd:COG0022 163 rdddPviF-LEHKR----LYRLKGEVPEEDY----TVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVI 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503394266 538 NARFLRPLDTDVILKAVRECGFVVTVEENTLCGGFGSTV-----------LEAAndaglptnnIKRLGIPDRFI 600
Cdd:COG0022 234 DLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIaariaeeafdyLDAP---------VKRVTGPDTPI 298
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
321-481 |
8.88e-36 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 132.29 E-value: 8.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 321 PAYTNIASKTIYDAMERDSKVVVMTAAMCAGNDL---GRIRDDFPQRFFDTGICEAHAVAFAAGMAKSG--MKPIVDIYS 395
Cdd:pfam02779 3 IATRKASGEALAELAKRDPRVVGGGADLAGGTFTvtkGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGplLPPVEATFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 396 TFLQRSFDHIFQEVALQNLPVVFCMDRAGLC-GPDGPTHHGVFDNTYMRTFPNITVMAPGDTADLQAMIPFSLEHDG--P 472
Cdd:pfam02779 83 DFLNRADDAIRHGAALGKLPVPFVVTRDPIGvGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGrkP 162
|
....*....
gi 503394266 473 ISIRYPKAN 481
Cdd:pfam02779 163 VVLRLPRQL 171
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
331-574 |
1.45e-35 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 137.42 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 331 IYDAMERDSKVVVMtaamcaGNDLGR----------IRDDF-PQRFFDTGICEAHAVAFAAGMAKSGMKPIVDI-YSTFL 398
Cdd:PTZ00182 45 LDEELARDPKVFVL------GEDVAQyggvykctkgLLDKYgPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 399 QRSFDHIFQEVA--------LQNLPVVFcmdRA--GLCGPDGPTHHGVFDNTYMRTfPNITVMAPGDTADLQAMIPFSLE 468
Cdd:PTZ00182 119 FPAFDQIVNEAAkyrymsggQFDCPIVI---RGpnGAVGHGGAYHSQSFEAYFAHV-PGLKVVAPSDPEDAKGLLKAAIR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 469 HDGPISIRYPKA--NAVTVERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLD 546
Cdd:PTZ00182 195 DPNPVVFFEPKLlyRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWD 274
|
250 260
....*....|....*....|....*...
gi 503394266 547 TDVILKAVRECGFVVTVEENTLCGGFGS 574
Cdd:PTZ00182 275 RETIVKSVKKTGRCVIVHEAPPTCGIGA 302
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
497-616 |
1.02e-31 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 119.24 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 497 GKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVVTVEENTLCGGFGSTV 576
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 503394266 577 LEAAND---AGLPTnNIKRLGIPDrFIEHGNRSELLGELGLDA 616
Cdd:pfam02780 81 AAALAEeafDGLDA-PVLRVGGPD-FPEPGSADELEKLYGLTP 121
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
335-576 |
1.70e-30 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 122.14 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 335 MERDSKVVVMtaamcaGNDLGR----------IRDDF-PQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIYS-TFLQRSF 402
Cdd:PRK09212 18 MERDPKVFLM------GEEVGEyqgaykvtqgLLEQFgPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFSMQAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 403 DHIFQEVALQN--------LPVVFcmdRaglcGPDGPT------HHGVFDNTYMRtFPNITVMAPGDTADLQAMIPFSLE 468
Cdd:PRK09212 92 DQIVNSAAKTNymsggqlkCPIVF---R----GPNGAAarvaaqHSQCYAAWYSH-IPGLKVVAPYFAADCKGLLKTAIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 469 HDGP-ISIRYPKANAVTVERENEVAPIELGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDT 547
Cdd:PRK09212 164 DPNPvIFLENEILYGHSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDT 243
|
250 260
....*....|....*....|....*....
gi 503394266 548 DVILKAVRECGFVVTVEENTLCGGFGSTV 576
Cdd:PRK09212 244 ETIIESVKKTNRLVVVEEGWPFAGVGAEI 272
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
310-576 |
3.08e-27 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 113.38 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 310 GDAIPRPKGSVPAYTNIASK-TIYDA--------MERDSKVVVMtaamcaGNDLGRIRDDF-----------PQRFFDTG 369
Cdd:PLN02683 7 RRTRPAAAAAARGYASAAKEmTVRDAlnsaldeeMSADPKVFIM------GEEVGEYQGAYkitkgllqkygPDRVLDTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 370 ICEAHAVAFAAGMAKSGMKPIVDIYS-TFLQRSFDHIFQEVALQN--------LPVVFcmdRaglcGPDGPT------HH 434
Cdd:PLN02683 81 ITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDHIINSAAKTNymsagqisVPIVF---R----GPNGAAagvgaqHS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 435 GVFDNTYMrTFPNITVMAPGDTADLQAMIPFSLEHDGPI-----SIRYPKANAVTVERENEVAPIELGKSEVLQWGTDGM 509
Cdd:PLN02683 154 QCFAAWYS-SVPGLKVLAPYSSEDARGLLKAAIRDPDPVvflenELLYGESFPVSAEVLDSSFVLPIGKAKIEREGKDVT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503394266 510 IVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVVTVEENTLCGGFGSTV 576
Cdd:PLN02683 233 IVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEI 299
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
243-539 |
1.95e-21 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 98.67 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 243 FEEMGFRYIgPVDGHDLDALRKYLEMVKDIKGPTLLHVFTEKGKGFkPASEDPVTFH-SPSPFD-------------RTD 308
Cdd:PRK05899 209 FEAYGWHVI-EVDGHDVEAIDAAIEEAKASTKPTLIIAKTIIGKGA-PNKEGTHKVHgAPLGAEeiaaakkelgwdyRKA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 309 DGDAI-----PRP---------KGSVpaYTNIAsktiydamerDSKVVVmtaamcagndlgriRDDFPQRFFDTGICEAH 374
Cdd:PRK05899 287 SGKALnalakALPelvggsadlAGSN--NTKIK----------GSKDFA--------------PEDYSGRYIHYGVREFA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 375 AVAFAAGMAKSGM-KPIVdiySTFLQ---RSFDhiFQEV-ALQNLPVVFCM--DRAGLcGPDGPTHHGVFDNTYMRTFPN 447
Cdd:PRK05899 341 MAAIANGLALHGGfIPFG---GTFLVfsdYARN--AIRLaALMKLPVIYVFthDSIGV-GEDGPTHQPVEQLASLRAIPN 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 448 ITVMAPGD---TADL-QAMIpfsLEHDGPISIRYPKANAVTVERENEVAPIELGKSEVLQwGTDGMIVCFGALLPECVKA 523
Cdd:PRK05899 415 LTVIRPADaneTAAAwKYAL---ERKDGPSALVLTRQNLPVLERTAQEEGVAKGGYVLRD-DPDVILIATGSEVHLALEA 490
|
330
....*....|....*.
gi 503394266 524 AEKLQKDGLDVGVINA 539
Cdd:PRK05899 491 ADELEAEGIKVRVVSM 506
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
331-479 |
1.22e-19 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 85.86 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 331 IYDAMERDSKVVVMTAAMCAGNDLGRIRDDFPQRFFDTGICEAHAVAFAAGMAKSGMKPIVDIY-STFLQRSFDHIFqEV 409
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAINGLA-DA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503394266 410 ALQNLPVVFCMDRAGLCGPDGPTHHGVFDNTYMRTFPNITVMAPgDTADLQAMIPFSLEHD----GPISIRYPK 479
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSP-SPAELPAGIDHAIRTAyasqGPVVVRLPR 154
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
289-582 |
4.63e-19 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 90.36 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 289 KPASEDPVTFHSPSPFDRTDDGDAIPRPKGS-------VPAYTNIASKTIYDA--------MERDSKVVVMtaamcaGND 353
Cdd:PRK11892 95 AEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAevaadpdIPAGTEMVTMTVREAlrdamaeeMRRDEDVFVM------GEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 354 LGR----------IRDDF-PQRFFDTGICEaHAVA-FAAGMAKSGMKPIVDiYSTF---LQrSFDHIFQEVALQNL---- 414
Cdd:PRK11892 169 VAEyqgaykvtqgLLQEFgARRVIDTPITE-HGFAgIGVGAAFAGLKPIVE-FMTFnfaMQ-AIDQIINSAAKTLYmsgg 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 415 ----PVVFcmdRaglcGPDGPT------HHGVFDNTYMRTfPNITVMAPGDTAD----LQAMI----P--FsLEHDgpis 474
Cdd:PRK11892 246 qmgcPIVF---R----GPNGAAarvaaqHSQDYAAWYSHI-PGLKVVAPYSAADakglLKAAIrdpnPviF-LENE---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 475 IRYPKANAVTvERENEVAPIelGKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAV 554
Cdd:PRK11892 313 ILYGQSFDVP-KLDDFVLPI--GKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESV 389
|
330 340 350
....*....|....*....|....*....|..
gi 503394266 555 RECGFVVTVEENTLCGGFGS----TVLEAAND 582
Cdd:PRK11892 390 KKTNRLVTVEEGWPQSGVGAeiaaRVMEQAFD 421
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
331-473 |
1.15e-14 |
|
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132919 [Multi-domain] Cd Length: 167 Bit Score: 72.13 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 331 IYDAMERDSKVVVMtaamcaGNDLGR----------IRDDF-PQRFFDTGICEAHAVAFAAGMAKSGMKPIVDI-YSTFL 398
Cdd:cd07036 7 LDEEMERDPRVVVL------GEDVGDyggvfkvtkgLLDKFgPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 399 QRSFDHIFQEVA--------LQNLPVVFCMDRAGLCGpDGPTHHGVFDNTYMrTFPNITVMAPGDTADLQAMIPFSLEHD 470
Cdd:cd07036 81 LPAFDQIVNEAAklrymsggQFKVPIVIRGPNGGGIG-GGAQHSQSLEAWFA-HIPGLKVVAPSTPYDAKGLLKAAIRDD 158
|
...
gi 503394266 471 GPI 473
Cdd:cd07036 159 DPV 161
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
329-582 |
4.11e-11 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 64.76 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 329 KTIYDAMERDSKVVVMtaamcaGNDLG------RIRDDFPQ-----RFFDTGICEAHAVAFAAGMAKSGMKPIVD-IYST 396
Cdd:CHL00144 12 EAIDEEMARDPRVFVI------GEDVGhyggsyKVTKGLHEkygdlRVLDTPIAENSFTGMAIGAAMTGLRPIVEgMNMG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 397 FLQRSFDHIFQEVALQ--------NLPVVfcmdragLCGPDG-----PTHHGVFDNTYMRTFPNITVMAPGDTADLQAMI 463
Cdd:CHL00144 86 FLLLAFNQISNNAGMLhytsggnfTIPIV-------IRGPGGvgrqlGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 464 PFSLEHDGPI-----SIRYP-KANavtVERENEVAPIElgKSEVLQWGTDGMIVCFGALLPECVKAAEKLQKDGLDVGVI 537
Cdd:CHL00144 159 KSAIRSNNPViffehVLLYNlKEE---IPDNEYLLPLE--KAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEII 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 503394266 538 NARFLRPLDTDVILKAVRECGFVVTVEENTLCGGFGSTVLEAAND 582
Cdd:CHL00144 234 DLISLKPLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINE 278
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
29-305 |
4.07e-08 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 54.82 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 29 EIREALCQIVER-KPAHFASNLGVVELCLAL---HLVFD------FEKDRLIWDTGHQ---IYPHKLITGRFSRFE--TI 93
Cdd:cd02012 2 RIRRLSIDMVQKaGSGHPGGSLSAADILAVLyfkVLKYDpadpkwPNRDRFVLSKGHAspaLYAVLALAGYLPEEDlkTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 94 RDRGGLM-GFPNPNESPYDLFMTGHAGASVSTVLGLQAADDLLFEDGRkSVAVIGDGALPSGVVFEAMNNAVGLKKDILV 172
Cdd:cd02012 82 RQLGSRLpGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYR-VYVLLGDGELQEGSVWEAASFAGHYKLDNLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 173 ILNDNqmgicprvgglatyldnarvapfynglkrdiawalNKVPMVGNSVE-HALSNMKDAvktllhggrlFEEMGFRYI 251
Cdd:cd02012 161 AIVDS-----------------------------------NRIQIDGPTDDiLFTEDLAKK----------FEAFGWNVI 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 503394266 252 gPVDGHDLDALRKYLEMVKDIKG-PTLLHVFTEKGKGFkPASEDPVTFHSPSPFD 305
Cdd:cd02012 196 -EVDGHDVEEILAALEEAKKSKGkPTLIIAKTIKGKGV-PFMENTAKWHGKPLGE 248
|
|
| PLN02790 |
PLN02790 |
transketolase |
364-537 |
2.28e-06 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 50.79 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 364 RFfdtGICEAHAVAFAAGMA--KSGMKPIVdiySTFLQRS--FDHIFQEVALQNLPVVFCM--DRAGLcGPDGPTHHGVF 437
Cdd:PLN02790 396 RF---GVREHGMGAICNGIAlhSSGLIPYC---ATFFVFTdyMRAAMRLSALSEAGVIYVMthDSIGL-GEDGPTHQPIE 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 438 DNTYMRTFPNITVMAPGDTADLQAMIPFSLEH-DGPISI---RYPKAN-----AVTVERENEVAPIELGKSEvlqwgTDG 508
Cdd:PLN02790 469 HLASLRAMPNILMLRPADGNETAGAYKVAVTNrKRPTVLalsRQKVPNlpgtsIEGVEKGGYVISDNSSGNK-----PDL 543
|
170 180
....*....|....*....|....*....
gi 503394266 509 MIVCFGALLPECVKAAEKLQKDGLDVGVI 537
Cdd:PLN02790 544 ILIGTGSELEIAAKAAKELRKEGKKVRVV 572
|
|
| PFOR_II |
pfam17147 |
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
510-594 |
2.56e-05 |
|
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.
Pssm-ID: 407280 [Multi-domain] Cd Length: 102 Bit Score: 43.40 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 510 IVCFGALLPECVKAAEKLQKDGLDVGVINARFLRPLDTDVILKAVRECGFVVTVEENTLCGGFGSTVLE---AANDAGLP 586
Cdd:pfam17147 5 IVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEELKELLAGVKKVVVLDRNISFGSPGQLGTEvkaALYDSDPP 84
|
....*....
gi 503394266 587 T-NNIKRLG 594
Cdd:pfam17147 85 VvNFIAGLG 93
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
357-455 |
3.72e-04 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 43.51 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503394266 357 IRDDFPQ-RFFDTGICEAHAVAFAAGM-AKSGMKPIVdiySTFLQrSFDHIFQEV---ALQNLPVVFCM--DRAGLcGPD 429
Cdd:PTZ00089 396 FTKASPEgRYIRFGVREHAMCAIMNGIaAHGGFIPFG---ATFLN-FYGYALGAVrlaALSHHPVIYVAthDSIGL-GED 470
|
90 100
....*....|....*....|....*.
gi 503394266 430 GPTHHGVFDNTYMRTFPNITVMAPGD 455
Cdd:PTZ00089 471 GPTHQPVETLALLRATPNLLVIRPAD 496
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
138-181 |
2.26e-03 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 40.56 E-value: 2.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503394266 138 DGRKSVAV--IGDGALPSGVVFEAMNNAVGLKKDILVILNDNQMGI 181
Cdd:cd02000 123 RGEDRVAVcfFGDGATNEGDFHEALNFAALWKLPVIFVCENNGYAI 168
|
|
| |
